Amyloid-like protein inclusions in tobacco transgenic plants.

The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the struc...

Full description

Bibliographic Details
Main Authors: Anna Villar-Piqué, Raimon Sabaté, Oriol Lopera, Jordi Gibert, Josep Maria Torne, Mireya Santos, Salvador Ventura
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2010-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC2964307?pdf=render
_version_ 1818030572446941184
author Anna Villar-Piqué
Raimon Sabaté
Oriol Lopera
Jordi Gibert
Josep Maria Torne
Mireya Santos
Salvador Ventura
author_facet Anna Villar-Piqué
Raimon Sabaté
Oriol Lopera
Jordi Gibert
Josep Maria Torne
Mireya Santos
Salvador Ventura
author_sort Anna Villar-Piqué
collection DOAJ
description The formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the structure of the inclusions formed by maize transglutaminase (TGZ) in the chloroplasts of tobacco transplastomic plants and demonstrate that they have an amyloid-like nature. Together with the evidence of amyloid structures in bacteria and fungi our data argue that amyloid formation is likely a ubiquitous process occurring across the different kingdoms of life. The discovery of amyloid conformations inside inclusions of genetically modified plants might have implications regarding their use for human applications.
first_indexed 2024-12-10T05:37:43Z
format Article
id doaj.art-40033e8d10864b68b392850371bb84c6
institution Directory Open Access Journal
issn 1932-6203
language English
last_indexed 2024-12-10T05:37:43Z
publishDate 2010-01-01
publisher Public Library of Science (PLoS)
record_format Article
series PLoS ONE
spelling doaj.art-40033e8d10864b68b392850371bb84c62022-12-22T02:00:22ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-01-01510e1362510.1371/journal.pone.0013625Amyloid-like protein inclusions in tobacco transgenic plants.Anna Villar-PiquéRaimon SabatéOriol LoperaJordi GibertJosep Maria TorneMireya SantosSalvador VenturaThe formation of insoluble protein deposits in human tissues is linked to the onset of more than 40 different disorders, ranging from dementia to diabetes. In these diseases, the proteins usually self-assemble into ordered β-sheet enriched aggregates known as amyloid fibrils. Here we study the structure of the inclusions formed by maize transglutaminase (TGZ) in the chloroplasts of tobacco transplastomic plants and demonstrate that they have an amyloid-like nature. Together with the evidence of amyloid structures in bacteria and fungi our data argue that amyloid formation is likely a ubiquitous process occurring across the different kingdoms of life. The discovery of amyloid conformations inside inclusions of genetically modified plants might have implications regarding their use for human applications.http://europepmc.org/articles/PMC2964307?pdf=render
spellingShingle Anna Villar-Piqué
Raimon Sabaté
Oriol Lopera
Jordi Gibert
Josep Maria Torne
Mireya Santos
Salvador Ventura
Amyloid-like protein inclusions in tobacco transgenic plants.
PLoS ONE
title Amyloid-like protein inclusions in tobacco transgenic plants.
title_full Amyloid-like protein inclusions in tobacco transgenic plants.
title_fullStr Amyloid-like protein inclusions in tobacco transgenic plants.
title_full_unstemmed Amyloid-like protein inclusions in tobacco transgenic plants.
title_short Amyloid-like protein inclusions in tobacco transgenic plants.
title_sort amyloid like protein inclusions in tobacco transgenic plants
url http://europepmc.org/articles/PMC2964307?pdf=render
work_keys_str_mv AT annavillarpique amyloidlikeproteininclusionsintobaccotransgenicplants
AT raimonsabate amyloidlikeproteininclusionsintobaccotransgenicplants
AT oriollopera amyloidlikeproteininclusionsintobaccotransgenicplants
AT jordigibert amyloidlikeproteininclusionsintobaccotransgenicplants
AT josepmariatorne amyloidlikeproteininclusionsintobaccotransgenicplants
AT mireyasantos amyloidlikeproteininclusionsintobaccotransgenicplants
AT salvadorventura amyloidlikeproteininclusionsintobaccotransgenicplants